ArticleProceedings of the National Academy of Sciences of the United States of America2011
LRRC52 (leucine-rich-repeat-containing protein 52), a testis-specific auxiliary subunit of the alkalization-activated Slo3 channel.
Article in Proceedings of the National Academy of Sciences of the United States of America, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 57 papers.
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Who cites it
57 citing papers in PubMed, 92 citations in OpenAlex.
- Zinc is a key regulator of the sperm-specific KeLife · 2026Article
- LRRC71 is essential for sperm motility, fertilization, and male fertility.The Journal of biological chemistry · 2026Article
- Molecular insight into transcriptome profiling of aerobic exercise induced changes in aged skeletal muscle.npj aging · 2026Article
- Review
- Transmembrane determinants of voltage-gating differences between BK (Slo1) and Slo3 channels.Biophysical journal · 2024Article
- pH Homeodynamics and Male Fertility: A Coordinated Regulation of Acid-Based Balance during Sperm Journey to Fertilization.Biomolecules · 2024Review
- NaInternational journal of molecular sciences · 2023Review
- Signaling Roleplay between Ion Channels during Mammalian Sperm Capacitation.Biomedicines · 2023Review
- SLO3: A Conserved Regulator of Sperm Membrane Potential.International journal of molecular sciences · 2023Review
- The Role of Sperm Membrane Potential and Ion Channels in Regulating Sperm Function.International journal of molecular sciences · 2023Review
- A selective inhibitor of the sperm-specific potassium channel SLO3 impairs human sperm function.Proceedings of the National Academy of Sciences of the United States of America · 2023Article
- The LRRC family of BK channel regulatory subunits: potential roles in health and disease.The Journal of physiology · 2022Review
- Homozygous mutation in SLO3 leads to severe asthenoteratozoospermia due to acrosome hypoplasia and mitochondrial sheath malformations.Reproductive biology and endocrinology : RB&E · 2022Article
- A Minimal Model Shows that a Positive Feedback Loop Between sNHE and SLO3 can Control Mouse Sperm Capacitation.Frontiers in cell and developmental biology · 2022Article
- Structure and Function of Ion Channels Regulating Sperm Motility-An Overview.International journal of molecular sciences · 2021Review
- Mathematical model reveals that heterogeneity in the number of ion transporters regulates the fraction of mouse sperm capacitation.PloS one · 2021Article
- Sperm ion channels and transporters in male fertility and infertility.Nature reviews. Urology · 2021Review
- The Slo3/Lrrc52 complex is sensitive to phosphoinositides.Channels (Austin, Tex.) · 2020Article
- Molecular Mechanism Underlying the Action ofFrontiers in cell and developmental biology · 2020Article
- Human sperm ion channel (dys)function: implications for fertilization.Human reproduction update · 2019Article
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Authors and funding
5 authors at 2 institutions in 1 country.
Funding
Abstract
KSper, a pH-dependent K(+) current in mouse spermatozoa that is critical for fertility, is activated by alkalization in the range of pH 6.4-7.2 at membrane potentials between -50 and 0 mV. Although the KSper pore-forming subunit is encoded by the Slo3 gene, heterologously expressed Slo3 channels are largely closed at potentials negative to 0 mV at physiological pH. Here we identify a Slo3-associating protein, LRRC52 (leucine-rich repeat-containing 52), that shifts Slo3 gating into a range of voltages and pH values similar to that producing KSper current activation. Message for LRRC52, a homolog of the Slo1-modifying LRRC26 protein, is enriched in testis relative to other homologous LRRC subunits and is developmentally regulated in concert with that for Slo3. LRRC52 protein is detected only in testis. It is markedly diminished from Slo3(-/-) testis and completely absent from Slo3(-/-) sperm, indicating that LRRC52 expression is critically dependent on the presence of Slo3. We also examined the ability of other LRRC subunits homologous to LRRC26 and LRRC52 to modify Slo3 currents. Although both LRRC26 and LRRC52 are able to modify Slo3 function, LRRC52 is the stronger modifier of Slo3 function. Effects of other related subunits were weaker or absent. We propose that LRRC52 is a testis-enriched Slo3 auxiliary subunit that helps define the specific alkalization dependence of KSper activation. Together, LRRC52 and LRRC26 define a new family of auxiliary subunits capable of critically modifying the gating behavior of Slo family channels.
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